Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1gene.[1][2]
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system.[2]
References
↑Lester D, Farquharson C, Russell G, Houston B (Apr 2000). "Identification of a family of noncanonical ubiquitin-conjugating enzymes structurally related to yeast UBC6". Biochem Biophys Res Commun. 269 (2): 474–80. doi:10.1006/bbrc.2000.2302. PMID10708578.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Lenk U, Yu H, Walter J, et al. (2002). "A role for mammalian Ubc6 homologues in ER-associated protein degradation". J. Cell Sci. 115 (Pt 14): 3007–14. PMID12082160.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID14574404.
Oh RS, Bai X, Rommens JM (2006). "Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress". J. Biol. Chem. 281 (30): 21480–90. doi:10.1074/jbc.M601843200. PMID16720581.